Results 41 to 50 of about 41,686 (254)

Acid sensing ion channel 1 in lateral hypothalamus contributes to breathing control. [PDF]

open access: yesPLoS ONE, 2012
Acid-sensing ion channels (ASICs) are present in neurons and may contribute to chemoreception. Among six subunits of ASICs, ASIC1 is mainly expressed in the central nervous system. Recently, multiple sites in the brain including the lateral hypothalamus (
Nana Song   +9 more
doaj   +1 more source

Acid-sensing ion channels in pain and disease [PDF]

open access: yesNature Reviews Neuroscience, 2013
Why do neurons sense extracellular acid? In large part, this question has driven increasing investigation on acid-sensing ion channels (ASICs) in the CNS and the peripheral nervous system for the past two decades. Significant progress has been made in understanding the structure and function of ASICs at the molecular level.
John A, Wemmie   +2 more
openaire   +2 more sources

Molecular basis of inhibition of acid sensing ion channel 1A by diminazene. [PDF]

open access: yesPLoS ONE, 2018
Acid-sensing ion channels (ASICs) are trimeric proton-gated cation permeable ion channels expressed primarily in neurons. Here we employed site-directed mutagenesis and electrophysiology to investigate the mechanism of inhibition of ASIC1a by diminazene.
Aram J Krauson   +2 more
doaj   +1 more source

Neurosensory mechanotransduction through acid‐sensing ion channels [PDF]

open access: yesJournal of Cellular and Molecular Medicine, 2013
AbstractAcid‐sensing ion channels (ASICs) are voltage‐insensitive cation channels responding to extracellular acidification. ASIC proteins have two transmembrane domains and a large extracellular domain. The molecular topology of ASICs is similar to that of the mechanosensory abnormality 4‐ or 10‐proteins expressed in touch receptor neurons and ...
Chen, Chih-Cheng, Wong, Chia-Wen
openaire   +2 more sources

Inherent dynamics of the acid-sensing ion channel 1 correlates with the gating mechanism. [PDF]

open access: yesPLoS Biology, 2009
The acid-sensing ion channel 1 (ASIC1) is a key receptor for extracellular protons. Although numerous structural and functional studies have been performed on this channel, the structural dynamics underlying the gating mechanism remains unknown.
Huaiyu Yang   +6 more
doaj   +1 more source

Acid-Sensing Ion Channels [PDF]

open access: yesCirculation Research, 2019
Rationale: Precise regulation of cerebral blood flow is critical for normal brain function. Insufficient cerebral blood flow contributes to brain dysfunction and neurodegeneration. Carbon dioxide (CO 2 ), via effects on local acidosis, is one of the most potent regulators of cerebral ...
Frank M, Faraci   +5 more
openaire   +2 more sources

Molecular modeling of mechanosensory ion channel structural and functional features.

open access: yesPLoS ONE, 2010
The DEG/ENaC (Degenerin/Epithelial Sodium Channel) protein family comprises related ion channel subunits from all metazoans, including humans. Members of this protein family play roles in several important biological processes such as transduction of ...
Renate Gessmann   +3 more
doaj   +1 more source

Hyperosmotic stress induces PARP1‐mediated HPF1‐dependent mono(ADP‐ribosyl)ation

open access: yesFEBS Letters, EarlyView.
Sorbitol‐induced hyperosmotic stress rapidly induces reversible mono(ADP‐ribosyl)ation (MARylation) on PARP1 without the signs of genotoxic signaling. We show that PARP1 autoMARylation is HPF1 dependent and forms hydroxylamine‐resistant O‐glycosidic linkages.
Anna Georgina Kopasz   +11 more
wiley   +1 more source

Endogenous Neuropeptide Nocistatin Is a Direct Agonist of Acid-Sensing Ion Channels (ASIC1, ASIC2 and ASIC3)

open access: yesBiomolecules, 2019
Acid-sensing ion channel (ASIC) channels belong to the family of ligand-gated ion channels known as acid-sensing (proton-gated) ion channels. Only a few activators of ASICs are known.
Dmitry I. Osmakov   +4 more
doaj   +1 more source

Modulation of Homer1 EVH1 domain internal dynamics by putative autism‐associated mutations

open access: yesFEBS Letters, EarlyView.
The putative autism‐associated M65I and S97L variants of the EVH1 domain of the postsynaptic scaffold protein Homer1 do not exhibit substantial changes in their overall structure or partner binding. Both of them, but especially the M65I variant, show altered internal dynamics relative to the wild‐type domain on the μs‐ms timescale, indicated by the ...
Fanni Farkas   +6 more
wiley   +1 more source

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